Chemical Property of Lactoferricin B
Chemical Property:
- PSA：1343.55000
- Density:1.48±0.1 g/cm3(Predicted)
- LogP:8.64960
- Storage Temp.:2-8°C
- Solubility.:H2O: 1 mg/mL
- XLogP3:-6.1
- Hydrogen Bond Donor Count:50
- Hydrogen Bond Acceptor Count:41
- Rotatable Bond Count:108
- Exact Mass:3124.6819537
- Heavy Atom Count:219
- Complexity:6910
- Purity/Quality:
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99% *data from raw suppliers
Lactoferrin *data from reagent suppliers
Safty Information:
- Pictogram(s):
B
- Hazard Codes:B
- Safety Statements:
22-24/25
- MSDS Files:
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Useful:
- Canonical SMILES:CCC(C)C(C(=O)NC(C(C)O)C(=O)NC(CS)C(=O)NC(C(C)C)C(=O)NC(CCCNC(=N)N)C(=O)NC(CCCNC(=N)N)C(=O)NC(C)C(=O)NC(CC1=CC=CC=C1)C(=O)O)NC(=O)C(CO)NC(=O)C2CCCN2C(=O)C(C)NC(=O)CNC(=O)C(CC(C)C)NC(=O)C(CCCCN)NC(=O)C(CCCCN)NC(=O)C(CCSC)NC(=O)C(CCCNC(=N)N)NC(=O)C(CC3=CNC4=CC=CC=C43)NC(=O)C(CCC(=O)N)NC(=O)C(CC5=CNC6=CC=CC=C65)NC(=O)C(CCCNC(=N)N)NC(=O)C(CCCNC(=N)N)NC(=O)C(CS)NC(=O)C(CCCCN)NC(=O)C(CC7=CC=CC=C7)N
- Isomeric SMILES:CC[C@H](C)[C@@H](C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)O)NC(=O)[C@H](CO)NC(=O)[C@@H]2CCCN2C(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC3=CNC4=CC=CC=C43)NC(=O)[C@H](CCC(=O)N)NC(=O)[C@H](CC5=CNC6=CC=CC=C65)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CS)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC7=CC=CC=C7)N
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description
Lactoferrin (formerly known as lactotransferrin) is a glycoprotein, and a member of a transferrin family, thus belonging to those proteins capable of binding and transferring Fe3+ ions (Metz-Boutique et al., 1984).It is produced by various mammals and is found in milk, nasal secretions, saliva and tears, and it is in great abundance in human colostrum. It has intrigued scientists for decades.Lactoferrin was first isolated by Sorensen and Sorensen from bovine milk in 1939. In 1960 it was concurrently determined to be the main iron binding protein in human milk by three independent laboratories (Groves, 1960; Johanson, 1960; Montreuil et al., 1960).Subsequent research identified lactoferrin in secretions from exocrine glands and in specific granules of neutrophils. Neutrophils after degranulation were obser ved to be the main source of lactoferrin in blood plasma (Iyer and Lonnerdal, 1993).Due to the increase in its concentration during most inflammatory reactions and some viral in fections, several authors classify lactoferrin as an acute-phase protein (Kanyshkova et al., 2001). Its concentration increases in all biological fluids, but the highest levels have been detected in the nidus of inflammation (Birgens, 1985).Thus, lactoferrin has a wide variety of biological functions, many of which do not appear to be connected with its iron binding ability (Brock, 2002).?
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Description
Lactoferrin, a granule-associated glycoprotein, is a cationic
protein with a high proportion of arginine and lysine at
the N-terminal region, with two glycosylation and several
iron-binding sites. Lactoferrin is highly antibacterial
against both gram-positive and gram-negative bacteria at
concentrations ranging from 3 to 50 μg/ml. It is believed
that these lethal effects are due to a direct interaction of
lactoferrin with the cell surface and subsequent disruption
of normal permeability functions of the membrane,
a so-called dissipation of proton motive force action (23).
Similarly, expression of an antimicrobial tachyplesin gene
from Asian horseshoe crabs led to antibacterial activity
against Erwinia spp. in transgenic potato (24).
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Uses
Lactoferrin was used in the fractionation of lactoperoxidase and lactoferrin from bovine whey using a cation exchange membrane. It was used in the determination of lactoferrin and immunoglobulin G in animal milks by new immunosensors. Lactoferrin was used to grow Streptococcus mutans in an iron-limiting medium. It was used to test if lactoferrin impedes epithelial cell adhesion in vitro.
